1F75

CRYSTAL STRUCTURE OF UNDECAPRENYL DIPHOSPHATE SYNTHASE FROM MICROCOCCUS LUTEUS B-P 26

Summary for 1F75

• Entry DOI: 10.2210/pdb1f75/pdb
• Descriptor: UNDECAPRENYL PYROPHOSPHATE SYNTHETASE, SULFATE ION (3 entities in total)
• Functional Keywords: parallel beta sheet, new fold for isoprenoid synthase, peptidoglycan synthesis, transferase
• Biological source: Micrococcus luteus
• Total number of polymer chains: 2
• Total formula weight: 58082.58

Authors

Fujihashi, M.,Zhang, Y.-W.,Higuchi, Y.,Li, X.-Y.,Koyama, T.,Miki, K. (deposition date: 2000-06-26, release date: 2001-03-28, Last modification date: 2024-02-07)

Primary citation

Fujihashi, M.,Zhang, Y.W.,Higuchi, Y.,Li, X.Y.,Koyama, T.,Miki, K.
Crystal structure of cis-prenyl chain elongating enzyme, undecaprenyl diphosphate synthase.
Proc.Natl.Acad.Sci.USA, 98:4337-4342, 2001

PubMed Abstract: Undecaprenyl diphosphate synthase (UPS) catalyzes the cis-prenyl chain elongation onto trans, trans-farnesyl diphosphate (FPP) to produce undecaprenyl diphosphate (UPP), which is indispensable for the biosynthesis of bacterial cell walls. We report here the crystal structure of UPS as the only three-dimensional structure among cis-prenyl chain elongating enzymes. The structure is classified into a protein fold family and is completely different from the so-called "isoprenoid synthase fold" that is believed to be a common structure for the enzymes relating to isoprenoid biosynthesis. Conserved amino acid residues among cis-prenyl chain elongating enzymes are located around a large hydrophobic cleft in the UPS structure. A structural P-loop motif, which frequently appears in the various kinds of phosphate binding site, is found at the entrance of this cleft. The catalytic site is determined on the basis of these structural features, from which a possible reaction mechanism is proposed.

PubMed: 11287651
DOI: 10.1073/pnas.071514398

Experimental method

X-RAY DIFFRACTION (2.2 Å)